ID   MATK_ARCUU              Reviewed;         506 AA.
AC   Q71ML5;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 45.
DE   RecName: Full=Maturase K {ECO:0000255|HAMAP-Rule:MF_01390};
DE   AltName: Full=Intron maturase {ECO:0000255|HAMAP-Rule:MF_01390};
GN   Name=matK {ECO:0000255|HAMAP-Rule:MF_01390};
OS   Arctostaphylos uva-ursi (Bearberry) (Arbutus uva-ursi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Ericaceae; Arbutoideae; Arctostaphylos.
OX   NCBI_TaxID=84009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kron K.A., Judd W.S., Stevens P.F., Crayn D.M., Anderberg A.A., Gadek P.A.,
RA   Quinn C.J., Luteyn J.L.;
RT   "A phylogenetic classification of Ericaceae: molecular and morphological
RT   evidence.";
RL   Bot. Rev. 68:335-423(2002).
CC   -!- FUNCTION: Usually encoded in the trnK tRNA gene intron. Probably
CC       assists in splicing its own and other chloroplast group II introns.
CC       {ECO:0000255|HAMAP-Rule:MF_01390}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the intron maturase 2 family. MatK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01390}.
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DR   EMBL; AF440411; AAQ04030.1; -; Genomic_DNA.
DR   PRIDE; Q71ML5; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   HAMAP; MF_01390; MatK; 1.
DR   InterPro; IPR024937; Domain_X.
DR   InterPro; IPR002866; Maturase_MatK.
DR   InterPro; IPR024942; Maturase_MatK_N.
DR   PANTHER; PTHR34811; PTHR34811; 2.
DR   Pfam; PF01348; Intron_maturas2; 1.
DR   Pfam; PF01824; MatK_N; 2.
PE   3: Inferred from homology;
KW   Chloroplast; mRNA processing; Plastid; RNA-binding; tRNA processing.
FT   CHAIN           1..506
FT                   /note="Maturase K"
FT                   /id="PRO_0000143253"
SQ   SEQUENCE   506 AA;  59698 MW;  EB5C064F1E78215D CRC64;
     MEEFKRDLEL DRSQQHDFIY PLIFQEYIYA LAHDRGLNRS IVLENPGYDN KSSLLIVKRL
     IIHLITQMYQ QNHFLFSAND SNKKKIVGYN TNFYSQMIFX GFAVVVEIPF SLXLLSSLEG
     KEIVKSQNFQ SXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXL
     RFFLHAYHNW NSLMTQKKSS FSFSKKNKRL FLFLYNFHVC EYESIFVFLR NQSSHLRSIS
     SETFLERIYF YRKIELXVFT KDFKAILWVF KXPFLHYVRY QGKSTLASKG TSLLMNKWKY
     YLVKFWQCYF YMWSQPRRIH INQLSNDSLD FLGYLSSVRL NPLMVRSQML KNAFLIGNAF
     XKFDTLVPII PMIGSLSKAK FGNVLGHPMN XSVWADLSNP DIMDRFXRXF RNLSHYHSGS
     LKKMSLYRVK YILRLSCART LARKHKSTVR AFLKRLGVGL LEEFFTEEEQ VFYLTFPKAS
     SSSGELYRRR IWYLDIICIN ELANHS